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  • Title: Unscrambling thermal stability and temperature adaptation in evolved variants of a cold-active lipase.
    Author: Gatti-Lafranconi P, Caldarazzo SM, Villa A, Alberghina L, Lotti M.
    Journal: FEBS Lett; 2008 Jun 25; 582(15):2313-8. PubMed ID: 18534193.
    Abstract:
    Directed evolution by error-prone PCR was applied to stabilize the cold-active lipase from Pseudomonas fragi (PFL). PFL displays high activity at 10 degrees C, but it is highly unstable even at moderate temperatures. After two rounds of evolution, a variant was generated with a 5-fold increase in half-life at 42 degrees C and a shift of 10 degrees C in the temperature optimum, nevertheless retaining cold-activity. The evolved lipase displayed specific activity higher than the wild type enzyme in the temperature range 29-42 degrees C. Biophysical measurements did not indicate any obvious difference between the improved variant and the wild type enzyme in terms of loss of secondary structure upon heat treatment, nor a shift in the apparent melting temperature.
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